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Platinum in PDB 9h49: Crystal Structure of the Adduct Between Human Serum Transferrin (Apo- Form) and Cisplatin

Protein crystallography data

The structure of Crystal Structure of the Adduct Between Human Serum Transferrin (Apo- Form) and Cisplatin, PDB code: 9h49 was solved by R.Troisi, F.Galardo, G.Ferraro, F.Sica, A.Merlino, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 80.84 / 3.52
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 88.184, 103.68, 200.283, 90, 90, 90
R / Rfree (%) 23.1 / 24.9

Platinum Binding Sites:

The binding sites of Platinum atom in the Crystal Structure of the Adduct Between Human Serum Transferrin (Apo- Form) and Cisplatin (pdb code 9h49). This binding sites where shown within 5.0 Angstroms radius around Platinum atom.
In total 4 binding sites of Platinum where determined in the Crystal Structure of the Adduct Between Human Serum Transferrin (Apo- Form) and Cisplatin, PDB code: 9h49:
Jump to Platinum binding site number: 1; 2; 3; 4;

Platinum binding site 1 out of 4 in 9h49

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Platinum binding site 1 out of 4 in the Crystal Structure of the Adduct Between Human Serum Transferrin (Apo- Form) and Cisplatin


Mono view


Stereo pair view

A full contact list of Platinum with other atoms in the Pt binding site number 1 of Crystal Structure of the Adduct Between Human Serum Transferrin (Apo- Form) and Cisplatin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Pt704

b:275.5
occ:0.80
N A:NH3705 2.1 263.1 0.8
O A:HOH802 2.1 236.9 0.8
N A:NH3706 2.1 243.4 0.8
SD A:MET256 2.2 210.1 1.0
CG A:MET256 3.2 191.6 1.0
CB A:MET256 3.5 172.6 1.0
CE A:MET256 3.7 192.8 1.0
CA A:MET256 4.6 156.3 1.0

Platinum binding site 2 out of 4 in 9h49

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Platinum binding site 2 out of 4 in the Crystal Structure of the Adduct Between Human Serum Transferrin (Apo- Form) and Cisplatin


Mono view


Stereo pair view

A full contact list of Platinum with other atoms in the Pt binding site number 2 of Crystal Structure of the Adduct Between Human Serum Transferrin (Apo- Form) and Cisplatin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Pt707

b:289.1
occ:0.80
O A:HOH801 2.1 255.5 0.8
N A:NH3708 2.1 263.1 0.8
N A:NH3709 2.1 264.9 0.8
SD A:MET499 2.2 217.9 1.0
CG A:MET499 3.5 197.4 1.0
CE A:MET499 3.7 207.5 1.0
CB A:MET499 4.1 193.8 1.0
OE1 A:GLU526 4.4 196.6 1.0
OH A:TYR514 4.5 231.7 1.0
O A:MET499 4.8 196.6 1.0
OE2 A:GLU526 4.8 192.1 1.0
CZ A:TYR514 4.8 226.7 1.0
CE1 A:TYR514 4.9 225.8 1.0

Platinum binding site 3 out of 4 in 9h49

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Platinum binding site 3 out of 4 in the Crystal Structure of the Adduct Between Human Serum Transferrin (Apo- Form) and Cisplatin


Mono view


Stereo pair view

A full contact list of Platinum with other atoms in the Pt binding site number 3 of Crystal Structure of the Adduct Between Human Serum Transferrin (Apo- Form) and Cisplatin within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Pt704

b:245.2
occ:0.65
N B:NH3706 2.1 235.0 0.7
N B:NH3705 2.1 224.7 0.7
O B:HOH802 2.1 214.4 0.7
SD B:MET256 2.2 205.4 1.0
CG B:MET256 2.9 185.0 1.0
CB B:MET256 3.2 170.4 1.0
CE B:MET256 3.5 196.8 1.0
CA B:MET256 4.8 155.5 1.0

Platinum binding site 4 out of 4 in 9h49

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Platinum binding site 4 out of 4 in the Crystal Structure of the Adduct Between Human Serum Transferrin (Apo- Form) and Cisplatin


Mono view


Stereo pair view

A full contact list of Platinum with other atoms in the Pt binding site number 4 of Crystal Structure of the Adduct Between Human Serum Transferrin (Apo- Form) and Cisplatin within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Pt707

b:203.1
occ:0.65
O B:HOH803 2.1 211.1 0.7
N B:NH3708 2.1 209.9 0.7
N B:NH3709 2.1 166.6 0.7
SD B:MET499 2.2 211.4 1.0
CB B:MET499 3.3 200.8 1.0
CG B:MET499 3.4 205.3 1.0
CE B:MET499 3.7 204.8 1.0
O B:MET499 3.8 190.4 1.0
CA B:MET499 4.6 195.0 1.0
C B:MET499 4.6 188.4 1.0
OH B:TYR514 5.0 200.2 1.0

Reference:

R.Troisi, F.Galardo, G.Ferraro, F.Sica, A.Merlino. Crystal Structure of the Adduct Between Human Serum Transferrin (Apo Form) and Cisplatin To Be Published.
Page generated: Sat Feb 8 23:58:55 2025

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